Abstract
The cascade of events that leads to vaccinia-induced actin polymerization requires Src-dependent tyrosine phosphorylation of the viral membrane protein A36R. We found that a localized outside-in signaling cascade induced by the viral membrane protein B5R is required to potently activate Src and induce A36R phosphorylation at the plasma membrane. In addition, Src-mediated phosphorylation of A36R regulated the ability of virus particles to recruit and release conventional kinesin. Thus, Src activity regulates the transition between cytoplasmic microtubule transport and actin-based motility at the plasma membrane.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Actins / metabolism*
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Animals
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Cell Line
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Cell Membrane / metabolism
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Cell Membrane / virology
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Chickens
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Consensus Sequence
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Enzyme Activation
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HeLa Cells
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Humans
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Kinesins / metabolism
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Membrane Glycoproteins / chemistry
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Membrane Glycoproteins / metabolism
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Microtubules / metabolism*
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Phosphorylation
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Phosphotyrosine / metabolism
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Recombinant Fusion Proteins / metabolism
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Vaccinia virus / genetics
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Vaccinia virus / metabolism*
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Vaccinia virus / physiology
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Viral Envelope Proteins / chemistry
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Viral Envelope Proteins / metabolism
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Viral Structural Proteins / metabolism*
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Virion / metabolism
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src-Family Kinases / metabolism*
Substances
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A36R protein, Vaccinia virus
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Actins
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Membrane Glycoproteins
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Recombinant Fusion Proteins
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Viral Envelope Proteins
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Viral Structural Proteins
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42kDa protein, Vaccinia virus
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Phosphotyrosine
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src-Family Kinases
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Kinesins